Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Receptor tyrosine-protein kinase erbB-3

Gene

Erbb3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5.By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei740ATPPROSITE-ProRule annotation1
Active sitei832Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi713 – 721ATPPROSITE-ProRule annotation9
Nucleotide bindingi786 – 788ATPPROSITE-ProRule annotation3
Nucleotide bindingi832 – 837ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • neuregulin binding Source: RGD
  • neuregulin receptor activity Source: RGD
  • transmembrane receptor protein tyrosine kinase activity Source: RGD

GO - Biological processi

  • axonogenesis Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • circadian rhythm Source: RGD
  • epidermal growth factor receptor signaling pathway Source: RGD
  • mammary gland involution Source: RGD
  • odontogenesis Source: RGD
  • positive regulation of glucose import Source: RGD
  • response to drug Source: RGD
  • response to wounding Source: RGD
  • skeletal muscle tissue development Source: RGD
  • tongue development Source: RGD
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: RGD

Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1 5301

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor tyrosine-protein kinase erbB-3 (EC:2.7.10.1)
Alternative name(s):
Proto-oncogene-like protein c-ErbB-3
Gene namesi
Name:Erbb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69323 Erbb3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 643ExtracellularSequence analysisAdd BLAST624
Transmembranei644 – 662HelicalSequence analysisAdd BLAST19
Topological domaini663 – 1339CytoplasmicSequence analysisAdd BLAST677

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001667320 – 1339Receptor tyrosine-protein kinase erbB-3Add BLAST1320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi186 ↔ 194By similarity
Disulfide bondi190 ↔ 202By similarity
Disulfide bondi210 ↔ 218By similarity
Disulfide bondi214 ↔ 226By similarity
Disulfide bondi227 ↔ 235By similarity
Disulfide bondi231 ↔ 243By similarity
Disulfide bondi246 ↔ 255By similarity
Glycosylationi250N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi259 ↔ 286By similarity
Disulfide bondi290 ↔ 301By similarity
Disulfide bondi305 ↔ 320By similarity
Disulfide bondi323 ↔ 327By similarity
Glycosylationi353N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi408N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi414N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi437N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi500 ↔ 509By similarity
Disulfide bondi504 ↔ 517By similarity
Disulfide bondi520 ↔ 529By similarity
Glycosylationi522N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi533 ↔ 549By similarity
Disulfide bondi552 ↔ 565By similarity
Disulfide bondi556 ↔ 573By similarity
Glycosylationi566N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi576 ↔ 585By similarity
Disulfide bondi589 ↔ 610By similarity
Disulfide bondi613 ↔ 621By similarity
Glycosylationi616N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi617 ↔ 629By similarity
Modified residuei684PhosphoserineCombined sources1
Modified residuei980PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ62799
PRIDEiQ62799

PTM databases

iPTMnetiQ62799
PhosphoSitePlusiQ62799

Interactioni

Subunit structurei

Monomer and homodimer. Heterodimer with each of the other ERBB receptors (Potential). Interacts with CSPG5, PA2G4, GRB7, MYOC and MUC1. Found in a ternary complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).By similarityCurated

GO - Molecular functioni

  • neuregulin binding Source: RGD

Protein-protein interaction databases

BioGridi248136, 4 interactors
DIPiDIP-41029N
ELMiQ62799
IntActiQ62799, 1 interactor
STRINGi10116.ENSRNOP00000006796

Structurei

3D structure databases

ProteinModelPortaliQ62799
SMRiQ62799
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini707 – 964Protein kinasePROSITE-ProRule annotationAdd BLAST258

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi183 – 259Cys-richAdd BLAST77

Domaini

The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1025 Eukaryota
ENOG410XNSR LUCA
HOGENOMiHOG000230982
HOVERGENiHBG000490
InParanoidiQ62799
KOiK05084
PhylomeDBiQ62799

Family and domain databases

Gene3Di3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016245 Tyr_kinase_EGF/ERB/XmrK_rcpt
PfamiView protein in Pfam
PF00757 Furin-like, 1 hit
PF14843 GF_recep_IV, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PIRSFiPIRSF000619 TyrPK_EGF-R, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00261 FU, 5 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY
60 70 80 90 100
KLYEKCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP
110 120 130 140 150
NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLKFTQLT EILSGGVYIE
160 170 180 190 200
KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG ANCPPCHEVC KGRCWGPGPD
210 220 230 240 250
DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD TDCFACRRFN
260 270 280 290 300
DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF
310 320 330 340 350
CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG
360 370 380 390 400
FVNCTKILGN LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ
410 420 430 440 450
SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS
460 470 480 490 500
AGRVYISANQ QLCYHHSLNW TRLLRGPSEE RLDIKYDRPL GECLAEGKVC
510 520 530 540 550
DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP REFVHEAQCF
560 570 580 590 600
SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
610 620 630 640 650
YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL
660 670 680 690 700
AVILMILGGS FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR
710 720 730 740 750
IFKETELRKL KVLGSGVFGT VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS
760 770 780 790 800
FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS LQLVTQYLPL GSLLDHVKQH
810 820 830 840 850
RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML KSPSQVQVAD
860 870 880 890 900
FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
910 920 930 940 950
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE
960 970 980 990 1000
NIRPTFKELA NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE
1010 1020 1030 1040 1050
AELEPELDLD LDLEAEEEGL ATSLGSALSL PTGTLTRPRG SQSLLSPSSG
1060 1070 1080 1090 1100
YMPMNQSSLG EACLDSAVLG GREQFSRPIS LHPIPRGRPA SESSEGHVTG
1110 1120 1130 1140 1150
SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV TPLSPPGLEE
1160 1170 1180 1190 1200
EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
1210 1220 1230 1240 1250
RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG
1260 1270 1280 1290 1300
TTPDEDYEYM NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP
1310 1320 1330
HVRYARLKTL RSLEATDSAF DNPDYWHSRL FPKANAQRT
Length:1,339
Mass (Da):147,546
Last modified:June 6, 2002 - v3
Checksum:i0AA5F2402BBFDF1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1028L → P in AAC53050 (PubMed:9030624).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29339 mRNA Translation: AAC28498.2
U52530 mRNA Translation: AAC53050.1
PIRiJC4387
RefSeqiNP_058914.2, NM_017218.3
UniGeneiRn.10228

Genome annotation databases

GeneIDi29496
KEGGirno:29496
UCSCiRGD:69323 rat

Similar proteinsi

Entry informationi

Entry nameiERBB3_RAT
AccessioniPrimary (citable) accession number: Q62799
Secondary accession number(s): Q62955
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 6, 2002
Last modified: June 20, 2018
This is version 149 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health